Evidence map›Paper›PMID 21878911›Full record

ArticleNature communications2011

Molecular mechanism for 3:1 subunit stoichiometry of rod cyclic nucleotide-gated ion channels.

Noah G Shuart, Yoni Haitin, Stacey S Camp, Kevin D Black, William N Zagotta

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
2.3field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Retinal Cyclic Nucleotide-Gated Channel Regulation by Calmodulin.International journal of molecular sciences · 2022
    Review
  11. Article
  12. Article
  13. Article
  14. The Natural History ofInternational journal of molecular sciences · 2022
    Article
  15. Genomic changes underlying repeated niche shifts in an adaptive radiation.Evolution; international journal of organic evolution · 2022
    Article
  16. Article
  17. Article
  18. Redefining the role of CaCell death & disease · 2022
    Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Noah G ShuartHoward Hughes Medical Institute and Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, USA.
Yoni Haitin
Stacey S Camp
Kevin D Black
William N Zagotta
University of Washington · US

Funding

GATING MECHANISMS OF RETINAL ROD CGMP-ACTIVATED CHANNELSR01EY010329 · NEI · UNIVERSITY OF WASHINGTON · PI ZAGOTTA, WILLIAM N · 1994 to 2023
$7.7M
Asymmetric flow FFF and Composition Gradient/Light Scattering SystemS10RR023748 · NCRR · YALE UNIVERSITY · PI FOLTA-STOGNIEW, EWA JOANNA · 2007 to 2007
$271k
NCRR NIH HHS S10 RR023748NEI NIH HHS R01 EY010329
6 · The paper itself

Abstract

Molecular determinants of ion channel tetramerization are well characterized, but those involved in heteromeric channel assembly are less clearly understood. The heteromeric composition of native channels is often precisely controlled. Cyclic nucleotide-gated (CNG) channels from rod photoreceptors exhibit a 3:1 stoichiometry of CNGA1 and CNGB1 subunits that tunes the channels for their specialized role in phototransduction. Here we show, using electrophysiology, fluorescence, biochemistry, and X-ray crystallography, that the mechanism for this controlled assembly is the formation of a parallel 3-helix coiled-coil domain of the carboxy-terminal leucine zipper region of CNGA1 subunits, constraining the channel to contain three CNGA1 subunits, followed by preferential incorporation of a single CNGB1 subunit. Deletion of the carboxy-terminal leucine zipper domain relaxed the constraint and permitted multiple CNGB1 subunits in the channel. The X-ray crystal structures of the parallel 3-helix coiled-coil domains of CNGA1 and CNGA3 subunits were similar, suggesting that a similar mechanism controls the stoichiometry of cone CNG channels.

Indexed as

Protein MultimerizationAnimalsCattleCrystallography, X-RayCyclic Nucleotide-Gated Cation ChannelsMolecular ConformationProtein Structure, TertiaryCNGA1 protein, humanCNGB1 protein, humanCyclic Nucleotide-Gated Cation Channels

Identifiers

PMID21878911
PMCPMC3265371
OpenAlexW1967194113

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.